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  • Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I.

Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I.

Biochimica et biophysica acta (1981-07-24)
T Masaki, T Fujihashi, K Nakamura, M Soejima
RÉSUMÉ

The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates. The binding affinity of alkylamines as determined by Ki was much stronger than that of the corresponding alkylguanidines.

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Sigma-Aldrich
Achromopeptidase from Lysobacter enzymogenes, partially purified powder, ≥20,000 units/mg solid